Mandelate racemase

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Mandelate racemase
mandelate racemase octamer, Pseudomonas putida
Identifiers
EC no. 5.1.2.2
CAS no. 2602087
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Mandelate racemase (EC 5.1.2.2) is a bacterial enzyme which catalyzes the interconversion of the enantiomers of mandelate via an enol intermediate. [1] This enzyme catalyses the following chemical reaction

(S)-mandelate ${\displaystyle \rightleftharpoons }$ (R)-mandelate

It is a member of the enolase superfamily of enzymes, along with muconate lactonizing enzyme and enolase.

Related Research Articles

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Muconate lactonizing enzymes are involved in the breakdown of lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates as a part of the β-ketoadipate pathway in soil microbes. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes. MLEs consist of several strands which have variable reaction favorable parts therefore the configuration of the strands affect its ability to accept protons. The bacterial MLEs belong to the enolase superfamily, several structures from which are known. MLEs have an identifying structure made up of two proteins and two Magnesium ions as well as various classes depending on whether it is bacterial or eukaryotic. The reaction mechanism that MLEs undergo are the reverse of beta-elimination in which the enolate alpha-carbon is protonated. MLEs can undergo mutations caused by a deletion of catB structural genes which can cause some bacteria to lose its functions such as the ability to grow. Additional mutations to MLEs can cause its structure and function to alter and could cause the conformation to change therefore making it an inactive enzyme that is unable to bind its substrate. There is another enzyme called Mandelate Racemase that is very similar to MLEs in the structural way as well as them both being a part of the enolase superfamily. They both have the same end product even though they undergo different chemical reactions in order to reach the end product.

The enolase superfamily is a superfamily of enzymes, members of which catalyse a range of reactions.

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o-Succinylbenzoate synthase (OSBS) (EC 4.2.1.113) is an enzyme encoded by the menC gene in E.coli, and catalyzes the dehydration of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to form 4-(2'-carboxyphenyl)-4-oxobutyrate, also called o-succinylbenzoate or OSB, hence the name of the enzyme. This reaction is the fourth step in the menaquinone biosynthetic pathway, which is used by bacteria to synthesize menaquinone, also known as vitamin K2.

References

1. Gunsalus CF, Stanier RY, Gunsalus IC (November 1953). "The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes". Journal of Bacteriology. 66 (5): 548–53. PMC  . PMID   13108854.